ArticleJournal of molecular modeling2011
Molecular dynamics simulation of oseltamivir resistance in neuraminidase of avian influenza H5N1 virus.
Article in Journal of molecular modeling, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 24 citations in OpenAlex.
- Integrated virtual screening and compound generation targeting H275Y mutation in the neuraminidase gene of oseltamivir-resistant influenza strains.Molecular diversity · 2025Article
- Identification of Residues That Affect Oligomerization and/or Enzymatic Activity of Influenza Virus H5N1 Neuraminidase Proteins.Journal of virology · 2016Article
- Molecular dynamics, monte carlo simulations, and langevin dynamics: a computational review.BioMed research international · 2015Review
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The outbreak of avian influenza virus H5N1 has raised a global concern because of its high virulence and mutation rate. Although two classes of antiviral drugs, M2 ion channel protein inhibitors and neuraminidase inhibitors, are expected to be important in controlling the early stages of a potential pandemic. Different strains of influenza viruses have differing degrees of resistance against the antivirals. In order to analyze the detailed information on the viral resistance, molecular dynamics simulations were carried out for the neuraminidase (NA) complex with oseltamivir. The carboxylate of Glu276 of H252Y NA faces toward the O-ethyl-propyl group of oseltamivir, Glu276 of wild-type NA adopts a conformation pointing away from the oseltamivir. τ2 and τ3 torsional angles fluctuation of the oseltamivir are relatively high for the H252Y mutant NA complex. In addition, there are fewer hydrogen bonds between the oseltamivir and H252Y mutation NA. The results show that H252Y mutation NA has high resistance against the drug.
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